Cytoplasmic nonpolysomal ribonucleoprotein complexes and translational control.
In this article, we discuss our attempts to establish the existence in the cytoplasm of regulatory molecules involved in translational control. Our studies have revealed the presence of cAMP independent protein kinase in the free mRNP complex capable of phosphorylating a Mr = 38 000 polypeptide, also part of the same complex. Both the kinase and the acceptor protein were found also as free proteins in the cytoplasmic pool. This kinase has been shown to be distinct from the heme regulated enzyme that phosphorylates the small subunit of eIF-2. Other regulatory molecules include small molecular weight RNAs found as part of an RNP complex. A 4S fraction isolated from this complex inhibited the translation of both capped and uncapped mRNAs in a cell-free protein synthesizing system. The biological role of the protein kinase and the 4S RNA fraction is considered.
D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D009698:Nucleoproteins / Q000235:genetics*; D010455:Peptides / Q000378:metabolism; D010766:Phosphorylation; D014176:Protein Biosynthesis; D011494:Protein Kinases / Q000378:metabolism*; D012333:RNA, Messenger / Q000235:genetics; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins / Q000235:genetics*
D002352:Carrier Proteins; D009698:Nucleoproteins; D010455:Peptides; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins; D011494:Protein Kinases